ID BPHL_HUMAN Reviewed; 291 AA.
AC Q86WA6; Q00306; Q13855; Q3KP51;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 178.
DE RecName: Full=Valacyclovir hydrolase;
DE Short=VACVase;
DE Short=Valacyclovirase;
DE EC=3.1.-.-;
DE AltName: Full=Biphenyl hydrolase-like protein;
DE AltName: Full=Biphenyl hydrolase-related protein;
DE Short=Bph-rp;
DE AltName: Full=Breast epithelial mucin-associated antigen;
DE Short=MCNAA;
DE Flags: Precursor;
GN Name=BPHL; Synonyms=MCNAA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 152-158;
RP 181-184 AND 209-214, AND TISSUE SPECIFICITY.
RC TISSUE=Mammary carcinoma;
RX PubMed=7759552; DOI=10.1074/jbc.270.21.12926;
RA Puente X.S., Lopez-Otin C.;
RT "Cloning and expression analysis of a novel human serine hydrolase with
RT sequence similarity to prokaryotic enzymes involved in the degradation of
RT aromatic compounds.";
RL J. Biol. Chem. 270:12926-12932(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Puente X.S.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary carcinoma;
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 182-280.
RX PubMed=2393862;
RA Larocca D., Peterson J.A., Walkup G., Urrea R., Ceriani R.L.;
RT "Cloning and sequencing of a complementary DNA encoding a M(r) 70,000 human
RT breast epithelial mucin-associated antigen.";
RL Cancer Res. 50:5925-5930(1990).
RN [7]
RP PROTEIN SEQUENCE OF 38-56, AND CHARACTERIZATION.
RX PubMed=12732646; DOI=10.1074/jbc.m302055200;
RA Kim I., Chu X.-Y., Kim S., Provoda C.J., Lee K.-D., Amidon G.L.;
RT "Identification of a human valacyclovirase: biphenyl hydrolase-like protein
RT as valacyclovir hydrolase.";
RL J. Biol. Chem. 278:25348-25356(2003).
RN [8]
RP CHROMOSOMAL LOCATION.
RX PubMed=9721218; DOI=10.1006/geno.1998.5351;
RA Puente X.S., Pendas A.M., Lopez-Otin C.;
RT "Structural characterization and chromosomal localization of the gene
RT encoding human biphenyl hydrolase-related protein (BPHL).";
RL Genomics 51:459-462(1998).
RN [9]
RP SUBUNIT.
RA Kim I.;
RL Submitted (DEC-2003) to UniProtKB.
RN [10]
RP SUBSTRATE SPECIFICITY.
RX PubMed=15832508; DOI=10.1021/mp0499757;
RA Kim I., Song X., Vig B.S., Mittal S., Shin H.-C., Lorenzi P.J.,
RA Amidon G.L.;
RT "A novel nucleoside prodrug-activating enzyme: substrate specificity of
RT biphenyl hydrolase-like protein.";
RL Mol. Pharm. 1:117-127(2004).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-126, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 38-291, FUNCTION, SUBUNIT, ACTIVE
RP SITES, AND MUTAGENESIS OF SER-139; ASP-244 AND HIS-272.
RX PubMed=18256025; DOI=10.1074/jbc.m709530200;
RA Lai L., Xu Z., Zhou J., Lee K.D., Amidon G.L.;
RT "Molecular basis of prodrug activation by human valacyclovirase, an alpha-
RT amino acid ester hydrolase.";
RL J. Biol. Chem. 283:9318-9327(2008).
CC -!- FUNCTION: Serine hydrolase that catalyzes the hydrolytic activation of
CC amino acid ester prodrugs of nucleoside analogs such as valacyclovir
CC and valganciclovir. Activates valacyclovir to acyclovir. May play a
CC role in detoxification processes. It is a specific alpha-amino acid
CC ester hydrolase that prefers small, hydrophobic, and aromatic side
CC chains and does not have a stringent requirement for the leaving group
CC other than preferring a primary alcohol. {ECO:0000269|PubMed:18256025}.
CC -!- SUBUNIT: Monomer. May also form homodimers.
CC {ECO:0000269|PubMed:18256025, ECO:0000269|Ref.9}.
CC -!- INTERACTION:
CC Q86WA6-2; P62508-3: ESRRG; NbExp=3; IntAct=EBI-21843491, EBI-12001340;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Beta;
CC IsoId=Q86WA6-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha;
CC IsoId=Q86WA6-2; Sequence=VSP_009115;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in liver and kidney and
CC lower levels in heart, intestine and skeletal muscle.
CC {ECO:0000269|PubMed:7759552}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; X81372; CAA57137.1; -; mRNA.
DR EMBL; AJ617684; CAE85120.1; -; mRNA.
DR EMBL; AL031963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55122.1; -; Genomic_DNA.
DR EMBL; BC106901; AAI06902.1; -; mRNA.
DR EMBL; X57653; CAA40859.1; -; mRNA.
DR CCDS; CCDS4483.2; -. [Q86WA6-1]
DR CCDS; CCDS78105.1; -. [Q86WA6-2]
DR PIR; A56716; A56716.
DR RefSeq; NP_001289706.1; NM_001302777.1. [Q86WA6-2]
DR RefSeq; NP_004323.2; NM_004332.3. [Q86WA6-1]
DR PDB; 2OCG; X-ray; 1.75 A; A=38-291.
DR PDB; 2OCI; X-ray; 1.90 A; A=38-291.
DR PDB; 2OCK; X-ray; 1.85 A; A=38-291.
DR PDB; 2OCL; X-ray; 1.90 A; A=38-291.
DR PDBsum; 2OCG; -.
DR PDBsum; 2OCI; -.
DR PDBsum; 2OCK; -.
DR PDBsum; 2OCL; -.
DR AlphaFoldDB; Q86WA6; -.
DR SMR; Q86WA6; -.
DR BioGRID; 107138; 49.
DR IntAct; Q86WA6; 5.
DR STRING; 9606.ENSP00000369739; -.
DR ChEMBL; CHEMBL3308924; -.
DR DrugBank; DB03380; L-tyrosinamide.
DR ESTHER; human-BPHL; Valacyclovir-hydrolase.
DR MEROPS; S33.982; -.
DR iPTMnet; Q86WA6; -.
DR PhosphoSitePlus; Q86WA6; -.
DR SwissPalm; Q86WA6; -.
DR BioMuta; BPHL; -.
DR DMDM; 39931107; -.
DR EPD; Q86WA6; -.
DR jPOST; Q86WA6; -.
DR MassIVE; Q86WA6; -.
DR MaxQB; Q86WA6; -.
DR PaxDb; 9606-ENSP00000369739; -.
DR PeptideAtlas; Q86WA6; -.
DR ProteomicsDB; 70136; -. [Q86WA6-1]
DR ProteomicsDB; 70137; -. [Q86WA6-2]
DR Pumba; Q86WA6; -.
DR Antibodypedia; 24354; 139 antibodies from 24 providers.
DR DNASU; 670; -.
DR Ensembl; ENST00000380375.4; ENSP00000369734.3; ENSG00000137274.13. [Q86WA6-2]
DR Ensembl; ENST00000380379.10; ENSP00000369739.5; ENSG00000137274.13. [Q86WA6-1]
DR Ensembl; ENST00000434640.5; ENSP00000390472.1; ENSG00000137274.13. [Q86WA6-2]
DR GeneID; 670; -.
DR KEGG; hsa:670; -.
DR MANE-Select; ENST00000380379.10; ENSP00000369739.5; NM_004332.4; NP_004323.2.
DR UCSC; uc003mva.4; human. [Q86WA6-1]
DR AGR; HGNC:1094; -.
DR CTD; 670; -.
DR DisGeNET; 670; -.
DR GeneCards; BPHL; -.
DR HGNC; HGNC:1094; BPHL.
DR HPA; ENSG00000137274; Tissue enhanced (kidney, liver).
DR MIM; 603156; gene.
DR neXtProt; NX_Q86WA6; -.
DR OpenTargets; ENSG00000137274; -.
DR PharmGKB; PA25402; -.
DR VEuPathDB; HostDB:ENSG00000137274; -.
DR eggNOG; KOG2984; Eukaryota.
DR GeneTree; ENSGT00390000004746; -.
DR HOGENOM; CLU_020336_50_5_1; -.
DR InParanoid; Q86WA6; -.
DR OMA; RFPQLWA; -.
DR OrthoDB; 980241at2759; -.
DR PhylomeDB; Q86WA6; -.
DR TreeFam; TF318389; -.
DR PathwayCommons; Q86WA6; -.
DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR SABIO-RK; Q86WA6; -.
DR SignaLink; Q86WA6; -.
DR BioGRID-ORCS; 670; 11 hits in 1164 CRISPR screens.
DR ChiTaRS; BPHL; human.
DR EvolutionaryTrace; Q86WA6; -.
DR GenomeRNAi; 670; -.
DR Pharos; Q86WA6; Tbio.
DR PRO; PR:Q86WA6; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q86WA6; Protein.
DR Bgee; ENSG00000137274; Expressed in right lobe of liver and 168 other cell types or tissues.
DR ExpressionAtlas; Q86WA6; baseline and differential.
DR Genevisible; Q86WA6; HS.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0047658; F:alpha-amino-acid esterase activity; IDA:FlyBase.
DR GO; GO:0006520; P:amino acid metabolic process; TAS:ProtInc.
DR GO; GO:0009636; P:response to toxic substance; TAS:ProtInc.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR PANTHER; PTHR46331; VALACYCLOVIR HYDROLASE; 1.
DR PANTHER; PTHR46331:SF2; VALACYCLOVIR HYDROLASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000269|PubMed:12732646"
FT CHAIN 38..291
FT /note="Valacyclovir hydrolase"
FT /id="PRO_0000017841"
FT DOMAIN 62..181
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 139
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:18256025"
FT ACT_SITE 244
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037,
FT ECO:0000269|PubMed:18256025"
FT ACT_SITE 272
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037,
FT ECO:0000269|PubMed:18256025"
FT SITE 140
FT /note="Binding of alpha-amino group of substrate"
FT MOD_RES 86
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R164"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R164"
FT MOD_RES 126
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 126
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8R164"
FT MOD_RES 184
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R164"
FT MOD_RES 191
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8R164"
FT MOD_RES 191
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8R164"
FT MOD_RES 217
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R164"
FT MOD_RES 243
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R164"
FT MOD_RES 260
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8R164"
FT MOD_RES 260
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8R164"
FT MOD_RES 271
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8R164"
FT MOD_RES 271
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8R164"
FT VAR_SEQ 1..36
FT /note="MVAVLGGRGVLRLRLLLSALKPGIHVPRAGPAAAFG -> MPRNLLYSLLSS
FT HLSPHFS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7759552"
FT /id="VSP_009115"
FT MUTAGEN 139
FT /note="S->A: <0.1% of wild type activity."
FT /evidence="ECO:0000269|PubMed:18256025"
FT MUTAGEN 244
FT /note="D->N: <0.1% of wild type activity."
FT /evidence="ECO:0000269|PubMed:18256025"
FT MUTAGEN 272
FT /note="H->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:18256025"
FT CONFLICT 182
FT /note="V -> R (in Ref. 6; CAA40859)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="G -> A (in Ref. 6; CAA40859)"
FT /evidence="ECO:0000305"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:2OCG"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:2OCG"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2OCG"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2OCG"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:2OCG"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:2OCG"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:2OCG"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:2OCG"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:2OCG"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:2OCG"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:2OCG"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:2OCG"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:2OCG"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2OCG"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:2OCG"
FT HELIX 199..214
FT /evidence="ECO:0007829|PDB:2OCG"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:2OCG"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:2OCG"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:2OCG"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:2OCG"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:2OCG"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:2OCG"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:2OCG"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:2OCG"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:2OCG"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:2OCG"
SQ SEQUENCE 291 AA; 32543 MW; 830B948492160244 CRC64;
MVAVLGGRGV LRLRLLLSAL KPGIHVPRAG PAAAFGTSVT SAKVAVNGVQ LHYQQTGEGD
HAVLLLPGML GSGETDFGPQ LKNLNKKLFT VVAWDPRGYG HSRPPDRDFP ADFFERDAKD
AVDLMKALKF KKVSLLGWSD GGITALIAAA KYPSYIHKMV IWGANAYVTD EDSMIYEGIR
DVSKWSERTR KPLEALYGYD YFARTCEKWV DGIRQFKHLP DGNICRHLLP RVQCPALIVH
GEKDPLVPRF HADFIHKHVK GSRLHLMPEG KHNLHLRFAD EFNKLAEDFL Q
//
